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Biophys J, February 1998, p. 918-930, Vol. 74, No. 2
*Institut Curie,
The interaction of dodecyl maltoside with lipids was
investigated through the studies of solubilization and reconstitution processes. The solubilization of large unilamellar liposomes was analyzed through changes in turbidity and cryo-transmission electron microscopy. Solubilization was well described by the three-stage model
previously reported for other detergents, and the critical detergent/phospholipid ratios at which lamellar-to-micellar transition occurred (Rsat = 1 mol/mol) and finished
(Rsol = 1.6 mol/mol) were determined. The
vesicle-micelle transition was further observed in the vitrified
hydrated state by cryo-transmission electron microscopy. A striking
feature of the solubilization process by dodecyl maltoside was the
discovery of a new phase consisting of a very viscous "gel-like"
sample. It is shown that this equilibrium cohesive phase is composed of
long filamentous thread-like micelles, over microns in length. Similar
structures were observed upon solubilization of sonicated liposomes,
multilamellar liposomes, or biological Ca2+ ATPase
membranes. This "gel-like" phase was also visualized during the
process of liposome reconstitution after detergent removal from
lipid-dodecyl maltoside micelles. The rate of detergent removal, controlled through the use of SM2 Bio-Beads, was demonstrated to
drastically influence the morphology of reconstituted liposomes with a
propensity for multilamellar liposome formation upon slow transition
through the "gel-like" phase. Finally, on the basis of these
observations, the mechanisms of dodecyl maltoside-mediated reconstitution of bacteriorhodopsin were analyzed, and optimal conditions for reconstitution were defined.
Biophys J, February 1998, p. 918-930, Vol. 74, No. 2
© 1998 by the Biophysical Society 0006-3495/98/02/918/13 $2.00
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